5fn1 | pdb_00005fn1

Electron cryo-microscopy of filamentous flexible virus PepMV (Pepino Mosaic Virus)

spinqualitylabelsall models 5fn1, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fn1 is a 2 chain structure with sequence from Pepino mosaic virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Flexible filamentous viruses include economically important plant pathogens. Their viral particles contain several hundred copies of a helically arrayed coat protein (CP) protecting a (+)ssRNA. We describe here a structure at 3.9 A resolution, from electron cryomicroscopy, of Pepino mosaic virus (PepMV), a representative of the genus Potexvirus (family Alphaflexiviridae). Our results allow modeling of the CP and its interactions with viral RNA. The overall fold of PepMV CP resembles that of nucleoproteins (NPs) from the genus Phlebovirus (family Bunyaviridae), a group of enveloped (-)ssRNA viruses. The main difference between potexvirus CP and phlebovirus NP is in their C-terminal extensions, which appear to determine the characteristics of the distinct multimeric assemblies- a flexuous, helical rod or a loose ribonucleoprotein (RNP). The homology suggests gene transfer between eukaryotic (+) and (-)ssRNA viruses. The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses.,Agirrezabala X, Mendez-Lopez E, Lasso G, Sanchez-Pina MA, Aranda M, Valle M Elife. 2015 Dec 16;4. pii: e11795. doi: 10.7554/eLife.11795. PMID:26673077 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat protein

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